FMO DATABASE

FMODB ID: 4G35N

Calculation Name: 6UM9-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6UM9

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: SolutionNMR

Registration Date: 2025-10-06

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1306819.949635
FMO2-HF: Nuclear repulsion	1247085.33399
FMO2-HF: Total energy	-59734.615646
FMO2-MP2: Total energy	-59897.266804

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:SER)

Summations of interaction energy for fragment #1(A:1:SER)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-58.347	-54.959	0.27	-1.267	-2.391	-0.008

Interaction energy analysis for fragmet #1(A:1:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.890 / q_NPA : 0.928

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	GLU	-1	-0.830	-0.905	3.897	-40.214	-38.688	-0.006	-0.561	-0.959	-0.001
4	A	4	VAL	0	-0.015	0.004	2.571	2.130	3.528	0.247	-0.604	-1.041	-0.006
5	A	5	MET	0	-0.019	-0.009	3.143	5.868	6.332	0.029	-0.102	-0.391	-0.001
6	A	6	LYS	1	0.928	0.987	6.887	27.225	27.225	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.026	0.000	10.143	-0.434	-0.434	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.005	0.017	12.913	1.429	1.429	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.035	-0.033	7.498	-0.634	-0.634	0.000	0.000	0.000	0.000
10	A	10	ILE	0	0.030	0.012	10.222	1.996	1.996	0.000	0.000	0.000	0.000
11	A	11	ASN	0	0.005	0.002	10.994	-2.316	-2.316	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.051	0.014	12.022	-0.620	-0.620	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.031	0.012	10.643	1.025	1.025	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.889	0.947	5.726	41.425	41.425	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.034	0.012	11.236	0.092	0.092	0.000	0.000	0.000	0.000
16	A	16	MET	0	-0.018	0.010	14.087	1.062	1.062	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.842	-0.928	8.250	-34.327	-34.327	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.003	0.020	12.537	0.535	0.535	0.000	0.000	0.000	0.000
19	A	19	CYS	0	-0.118	-0.022	13.712	0.980	0.980	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.926	0.973	15.242	19.832	19.832	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.090	-0.061	11.170	0.385	0.385	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.953	-0.966	16.597	-15.568	-15.568	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.034	-0.034	18.579	0.838	0.838	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.061	-0.019	20.132	0.258	0.258	0.000	0.000	0.000	0.000
25	A	25	VAL	0	0.020	0.025	20.590	0.618	0.618	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.002	-0.007	20.238	-0.882	-0.882	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.897	-0.974	17.195	-17.890	-17.890	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.021	0.005	19.903	0.031	0.031	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.021	0.026	23.102	0.184	0.184	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.018	0.002	15.853	0.196	0.196	0.000	0.000	0.000	0.000
31	A	31	GLN	0	-0.025	-0.033	20.986	0.095	0.095	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.837	-0.912	22.341	-11.301	-11.301	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.014	-0.010	20.113	0.392	0.392	0.000	0.000	0.000	0.000
34	A	34	PHE	0	-0.023	-0.015	17.686	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.072	-0.052	23.545	0.627	0.627	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.011	-0.002	27.022	0.424	0.424	0.000	0.000	0.000	0.000
37	A	37	TRP	0	-0.018	-0.010	23.851	0.611	0.611	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.907	0.966	28.404	10.923	10.923	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.852	-0.930	30.834	-9.570	-9.570	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.005	-0.008	34.409	0.099	0.099	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.022	0.003	30.320	0.272	0.272	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.029	-0.018	33.688	-0.097	-0.097	0.000	0.000	0.000	0.000
43	A	43	ILE	0	-0.044	-0.021	28.864	-0.035	-0.035	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.012	-0.003	32.080	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.045	-0.020	28.151	0.446	0.446	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.939	0.952	30.083	9.239	9.239	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.839	-0.939	25.763	-11.819	-11.819	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.024	0.017	25.750	-0.496	-0.496	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.025	0.011	26.229	-0.264	-0.264	0.000	0.000	0.000	0.000
50	A	50	CYS	0	-0.061	-0.027	25.715	-0.197	-0.197	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.039	0.001	20.411	-0.383	-0.383	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.008	0.003	22.632	-0.431	-0.431	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.035	0.012	24.661	-0.210	-0.210	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.006	-0.017	17.937	-0.659	-0.659	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.003	0.013	21.149	-0.200	-0.200	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.946	0.975	22.826	11.889	11.889	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.903	0.952	16.905	15.998	15.998	0.000	0.000	0.000	0.000
58	A	59	LEU	0	0.051	0.013	18.209	-0.956	-0.956	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.871	-0.908	19.338	-14.347	-14.347	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.064	-0.029	14.089	-0.594	-0.594	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.048	-0.013	14.076	-1.671	-1.671	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.827	-0.914	14.501	-19.878	-19.878	0.000	0.000	0.000	0.000
63	A	64	GLN	0	0.038	0.026	16.297	1.075	1.075	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.875	-0.931	18.285	-15.061	-15.061	0.000	0.000	0.000	0.000
65	A	66	MET	0	-0.084	-0.032	17.493	0.821	0.821	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.023	-0.033	21.196	1.179	1.179	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.011	0.012	21.734	0.535	0.535	0.000	0.000	0.000	0.000
68	A	69	HIS	0	0.006	-0.008	21.634	-0.211	-0.211	0.000	0.000	0.000	0.000
69	A	70	HIS	1	0.839	0.893	24.357	12.915	12.915	0.000	0.000	0.000	0.000
70	A	71	GLY	0	0.010	-0.004	26.684	0.068	0.068	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.872	0.935	27.911	10.948	10.948	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.026	0.026	29.663	-0.077	-0.077	0.000	0.000	0.000	0.000
73	A	74	MET	0	0.068	0.025	30.657	-0.030	-0.030	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.914	-0.950	30.818	-9.344	-9.344	0.000	0.000	0.000	0.000
75	A	76	PHE	0	-0.056	-0.019	23.759	-0.104	-0.104	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.048	0.011	28.576	-0.200	-0.200	0.000	0.000	0.000	0.000
77	A	78	MET	0	-0.009	0.016	30.737	0.048	0.048	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.859	0.935	27.396	10.564	10.564	0.000	0.000	0.000	0.000
79	A	80	HIS	1	0.759	0.879	23.236	12.243	12.243	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.000	0.011	28.697	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.000	0.014	32.256	0.208	0.208	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.858	-0.937	34.389	-8.239	-8.239	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.916	-0.975	37.369	-7.716	-7.716	0.000	0.000	0.000	0.000
84	A	85	ALA	0	-0.049	-0.036	38.706	0.012	0.012	0.000	0.000	0.000	0.000
85	A	86	MET	0	-0.016	0.000	37.139	0.102	0.102	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.049	0.021	34.606	-0.088	-0.088	0.000	0.000	0.000	0.000
87	A	88	LYS	1	0.930	0.961	35.752	7.390	7.390	0.000	0.000	0.000	0.000
88	A	89	GLN	0	0.041	0.031	38.559	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.009	0.008	32.430	0.023	0.023	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.007	-0.006	33.272	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.966	-0.978	36.541	-7.410	-7.410	0.000	0.000	0.000	0.000
92	A	93	ILE	0	0.006	0.009	37.236	0.081	0.081	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.811	0.901	32.167	9.699	9.699	0.000	0.000	0.000	0.000
94	A	95	HIS	1	0.787	0.849	36.382	8.690	8.690	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.028	-0.004	39.847	0.231	0.231	0.000	0.000	0.000	0.000
96	A	97	CYS	0	-0.025	-0.006	34.914	0.364	0.364	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.815	-0.910	36.461	-8.515	-8.515	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.892	0.952	39.865	6.984	6.984	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.064	-0.032	42.700	0.211	0.211	0.000	0.000	0.000	0.000
100	A	101	ILE	0	-0.046	0.004	37.395	0.032	0.032	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.019	-0.018	40.293	0.098	0.098	0.000	0.000	0.000	0.000
102	A	103	ILE	0	0.036	0.026	38.314	-0.274	-0.274	0.000	0.000	0.000	0.000
103	A	104	VAL	0	-0.063	-0.034	37.224	0.215	0.215	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.019	-0.004	37.373	-0.181	-0.181	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.895	-0.950	37.093	-8.205	-8.205	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.817	-0.894	32.994	-9.939	-9.939	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.058	0.019	30.851	0.079	0.079	0.000	0.000	0.000	0.000
108	A	110	GLN	0	0.061	0.016	30.817	-0.267	-0.267	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.017	0.006	34.109	0.193	0.193	0.000	0.000	0.000	0.000
110	A	112	MET	0	0.006	0.005	28.299	0.191	0.191	0.000	0.000	0.000	0.000
111	A	113	LEU	0	-0.002	0.000	30.552	-0.077	-0.077	0.000	0.000	0.000	0.000
112	A	114	ASN	0	-0.036	-0.032	32.216	0.070	0.070	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.010	0.011	33.003	0.149	0.149	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.039	0.016	30.786	0.080	0.080	0.000	0.000	0.000	0.000
115	A	117	MET	0	-0.027	-0.017	32.825	-0.038	-0.038	0.000	0.000	0.000	0.000
116	A	119	PHE	0	0.049	0.007	31.912	0.109	0.109	0.000	0.000	0.000	0.000
117	A	120	LYS	1	0.877	0.934	30.422	10.230	10.230	0.000	0.000	0.000	0.000
118	A	121	ALA	0	-0.025	-0.004	34.792	0.064	0.064	0.000	0.000	0.000	0.000
119	A	122	GLU	-1	-0.823	-0.906	38.506	-7.342	-7.342	0.000	0.000	0.000	0.000
120	A	123	ILE	0	0.009	-0.018	32.899	0.086	0.086	0.000	0.000	0.000	0.000
121	A	124	HIS	0	-0.053	-0.008	37.413	-0.154	-0.154	0.000	0.000	0.000	0.000
122	A	125	LYS	1	0.768	0.874	38.407	7.484	7.484	0.000	0.000	0.000	0.000
123	A	126	LEU	0	-0.071	-0.019	38.178	0.227	0.227	0.000	0.000	0.000	0.000
124	A	127	ASP	-1	-0.942	-0.966	40.365	-7.422	-7.422	0.000	0.000	0.000	0.000
125	A	128	TRP	0	-0.014	-0.013	34.207	-0.188	-0.188	0.000	0.000	0.000	0.000
126	A	129	ALA	0	0.020	0.007	33.723	-0.039	-0.039	0.000	0.000	0.000	0.000
127	A	130	PRO	0	0.004	0.014	31.324	-0.178	-0.178	0.000	0.000	0.000	0.000
128	A	131	THR	0	-0.003	-0.013	26.246	-0.056	-0.056	0.000	0.000	0.000	0.000
129	A	132	LEU	0	0.035	0.000	24.389	0.044	0.044	0.000	0.000	0.000	0.000
130	A	133	ASP	-1	-0.875	-0.934	22.437	-13.621	-13.621	0.000	0.000	0.000	0.000
131	A	134	VAL	0	0.001	0.005	24.738	-0.036	-0.036	0.000	0.000	0.000	0.000
132	A	135	ALA	0	0.015	0.007	28.285	0.189	0.189	0.000	0.000	0.000	0.000
133	A	136	VAL	0	-0.016	-0.010	23.756	0.149	0.149	0.000	0.000	0.000	0.000
134	A	137	GLY	0	0.027	0.013	25.374	-0.045	-0.045	0.000	0.000	0.000	0.000
135	A	138	GLU	-1	-0.831	-0.954	26.176	-9.625	-9.625	0.000	0.000	0.000	0.000
136	A	139	LEU	0	-0.030	-0.009	29.088	0.132	0.132	0.000	0.000	0.000	0.000
137	A	140	LEU	0	-0.052	-0.022	23.461	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	141	ALA	0	-0.010	-0.010	26.826	-0.176	-0.176	0.000	0.000	0.000	0.000
139	A	142	ASP	-1	-0.874	-0.918	27.762	-9.158	-9.158	0.000	0.000	0.000	0.000
140	A	143	THR	-1	-0.891	-0.914	27.407	-9.617	-9.617	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:SER)